| MWexperimental | 53 | kDa |
| MWexpected | 60 | kDa |
| VPorod | 231 | nm3 |
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log I(s)
2.75×10-1
2.75×10-2
2.75×10-3
2.75×10-4
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s, nm-1
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How the central domain of dystrophin acts to bridge F-actin to sarcolemmal lipids.
Mias-Lucquin D, Dos Santos Morais R, Chéron A, Lagarrigue M, Winder SJ, Chenuel T, Pérez J, Appavou MS, Martel A, Alviset G, Le Rumeur E, Combet S, Hubert JF, Delalande O, J Struct Biol :107411 (2019) Europe PMCSASDFV4 – Conformation of R11-15 human dystrophin fragment in interaction with anionic phospholipid bicelles (SANS)
Dystrophin (R11-15 human dystrophin fragment)|
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Fits and models
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SANS data from solutions of the R11-15 human dystrophin fragment with anionic phospholipid bicelles in 20 mM Tris-d11, 150 mM NaCl, 0.1 mM EDTA-d16, in 100% v/v D2O, pH 7.1 were collected on the D22 beam line at the ILL (Grenoble, France) using a 3He multidetector 128 linear sensitive Reuter-Stokes detector at a wavelength of λ = 0.6 nm (l(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). One solute concentration of 5.60 mg/ml was measured at 22°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.
Data were collected at two sample detector positions: 1) 1.4 m for 5 min using a neutron wavelength of 0.6 nm and; 2) 8 m for 20 min using a neutron wavelength of 0.6 nm. Both datasets were recorded on the same sample at 5.6 mg/mL, measured at 22 °C.
Tags:
sans
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